Atomistry » Magnesium » PDB 1gpm-1h7l » 1gsa
Atomistry »
  Magnesium »
    PDB 1gpm-1h7l »
      1gsa »

Magnesium in PDB 1gsa: Structure of Glutathione Synthetase Complexed with Adp and Glutathione

Enzymatic activity of Structure of Glutathione Synthetase Complexed with Adp and Glutathione

All present enzymatic activity of Structure of Glutathione Synthetase Complexed with Adp and Glutathione:
6.3.2.3;

Protein crystallography data

The structure of Structure of Glutathione Synthetase Complexed with Adp and Glutathione, PDB code: 1gsa was solved by T.Hara, H.Kato, T.Nishioka, Y.Katsube, J.Oda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 87.250, 87.250, 169.580, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Glutathione Synthetase Complexed with Adp and Glutathione (pdb code 1gsa). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Glutathione Synthetase Complexed with Adp and Glutathione, PDB code: 1gsa:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1gsa

Go back to Magnesium Binding Sites List in 1gsa
Magnesium binding site 1 out of 2 in the Structure of Glutathione Synthetase Complexed with Adp and Glutathione


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Glutathione Synthetase Complexed with Adp and Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg319

b:22.7
occ:1.00
OE2 A:GLU281 2.0 31.8 1.0
O1A A:ADP317 2.0 22.2 1.0
OD2 A:ASP273 2.0 16.8 1.0
O A:HOH458 2.1 18.6 1.0
O4 A:SO4400 2.1 33.9 1.0
O3B A:ADP317 2.2 26.2 1.0
CD A:GLU281 3.1 26.1 1.0
CG A:ASP273 3.2 16.3 1.0
S A:SO4400 3.2 33.8 1.0
PA A:ADP317 3.2 23.8 1.0
PB A:ADP317 3.3 23.8 1.0
O2 A:SO4400 3.3 36.1 1.0
O3A A:ADP317 3.6 23.9 1.0
MG A:MG320 3.6 31.1 1.0
O1B A:ADP317 3.7 24.7 1.0
OD1 A:ASP273 3.7 15.2 1.0
CG A:GLU281 3.8 24.7 1.0
ND2 A:ASN235 3.8 28.8 1.0
OE1 A:GLU281 3.9 24.3 1.0
O A:HOH445 4.1 26.2 1.0
O3 A:SO4400 4.1 36.1 1.0
O1 A:SO4400 4.1 32.9 1.0
O5' A:ADP317 4.1 23.9 1.0
C5' A:ADP317 4.2 25.0 1.0
NH2 A:ARG225 4.2 27.9 1.0
CB A:ASP273 4.3 10.7 1.0
O2A A:ADP317 4.3 22.5 1.0
OD2 A:ASP208 4.3 13.7 1.0
ND2 A:ASN283 4.3 24.2 1.0
O2B A:ADP317 4.6 26.2 1.0
NH1 A:ARG225 4.6 26.6 1.0
NH2 A:ARG210 4.8 24.3 1.0
CG A:ASN235 4.8 29.3 1.0
CZ A:ARG225 4.9 27.6 1.0
O3' A:ADP317 4.9 26.8 1.0
CB A:GLU281 4.9 23.3 1.0

Magnesium binding site 2 out of 2 in 1gsa

Go back to Magnesium Binding Sites List in 1gsa
Magnesium binding site 2 out of 2 in the Structure of Glutathione Synthetase Complexed with Adp and Glutathione


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Glutathione Synthetase Complexed with Adp and Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg320

b:31.1
occ:1.00
O2 A:SO4400 1.9 36.1 1.0
OE2 A:GLU281 2.2 31.8 1.0
OD1 A:ASN283 2.3 28.8 1.0
O A:HOH513 2.4 21.3 1.0
CD A:GLU281 2.5 26.1 1.0
OE1 A:GLU281 2.6 24.3 1.0
O1B A:ADP317 2.7 24.7 1.0
S A:SO4400 2.9 33.8 1.0
ND2 A:ASN283 2.9 24.2 1.0
CG A:ASN283 3.0 23.5 1.0
O1 A:SO4400 3.1 32.9 1.0
O4 A:SO4400 3.4 33.9 1.0
MG A:MG319 3.6 22.7 1.0
O3B A:ADP317 3.7 26.2 1.0
CG A:GLU281 3.7 24.7 1.0
CB A:MET165 3.8 35.4 1.0
PB A:ADP317 3.8 23.8 1.0
OE1 A:GLU124 4.0 22.9 1.0
O3 A:SO4400 4.1 36.1 1.0
CA A:MET165 4.1 33.2 1.0
CB A:ASN283 4.4 19.1 1.0
CB2 A:GSH318 4.4 26.1 1.0
NZ A:LYS125 4.7 24.2 1.0
O3A A:ADP317 4.7 23.9 1.0
OD2 A:ASP273 4.7 16.8 1.0
CD A:GLU124 4.7 18.1 1.0
O1A A:ADP317 4.8 22.2 1.0
N A:GLY166 4.8 31.6 1.0
O A:GLY164 4.8 33.4 1.0
O2B A:ADP317 4.9 26.2 1.0
CB A:GLU281 4.9 23.3 1.0
NH2 A:ARG210 4.9 24.3 1.0
CB A:GLU124 4.9 13.9 1.0
CG A:MET165 4.9 37.2 1.0

Reference:

T.Hara, H.Kato, Y.Katsube, J.Oda. A Pseudo-Michaelis Quaternary Complex in the Reverse Reaction of A Ligase: Structure of Escherichia Coli B Glutathione Synthetase Complexed with Adp, Glutathione, and Sulfate at 2.0 A Resolution. Biochemistry V. 35 11967 1996.
ISSN: ISSN 0006-2960
PubMed: 8810901
DOI: 10.1021/BI9605245
Page generated: Mon Dec 14 05:58:21 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy